CN1312854A - Fast measuring device of enzymatic activity - Google Patents
Fast measuring device of enzymatic activity Download PDFInfo
- Publication number
- CN1312854A CN1312854A CN99809785A CN99809785A CN1312854A CN 1312854 A CN1312854 A CN 1312854A CN 99809785 A CN99809785 A CN 99809785A CN 99809785 A CN99809785 A CN 99809785A CN 1312854 A CN1312854 A CN 1312854A
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- CN
- China
- Prior art keywords
- reagent
- enzymic activity
- enzyme
- solid
- feed
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- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 230000002255 enzymatic effect Effects 0.000 title abstract 2
- 230000000694 effects Effects 0.000 claims abstract description 24
- 108090000790 Enzymes Proteins 0.000 claims abstract description 21
- 102000004190 Enzymes Human genes 0.000 claims abstract description 21
- 239000003153 chemical reaction reagent Substances 0.000 claims abstract description 13
- 238000013016 damping Methods 0.000 claims description 12
- 239000012530 fluid Substances 0.000 claims description 12
- 239000007787 solid Substances 0.000 claims description 10
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 9
- 239000000758 substrate Substances 0.000 claims description 8
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 claims description 6
- 239000007788 liquid Substances 0.000 claims description 5
- 239000007791 liquid phase Substances 0.000 claims description 5
- 238000000034 method Methods 0.000 claims description 5
- IVLXQGJVBGMLRR-UHFFFAOYSA-N 2-aminoacetic acid;hydron;chloride Chemical compound Cl.NCC(O)=O IVLXQGJVBGMLRR-UHFFFAOYSA-N 0.000 claims description 3
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 claims description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical group CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 claims description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 3
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 claims description 3
- GTZCVFVGUGFEME-IWQZZHSRSA-N cis-aconitic acid Chemical compound OC(=O)C\C(C(O)=O)=C\C(O)=O GTZCVFVGUGFEME-IWQZZHSRSA-N 0.000 claims description 3
- 235000019253 formic acid Nutrition 0.000 claims description 3
- 229960001269 glycine hydrochloride Drugs 0.000 claims description 3
- 239000001632 sodium acetate Substances 0.000 claims description 3
- 235000017281 sodium acetate Nutrition 0.000 claims description 3
- HLBBKKJFGFRGMU-UHFFFAOYSA-M sodium formate Chemical compound [Na+].[O-]C=O HLBBKKJFGFRGMU-UHFFFAOYSA-M 0.000 claims description 3
- 239000011324 bead Substances 0.000 claims description 2
- 239000007790 solid phase Substances 0.000 claims description 2
- 238000005259 measurement Methods 0.000 abstract description 5
- 235000021055 solid food Nutrition 0.000 abstract 1
- 229940088598 enzyme Drugs 0.000 description 16
- 239000002245 particle Substances 0.000 description 7
- 238000006243 chemical reaction Methods 0.000 description 5
- FYGDTMLNYKFZSV-URKRLVJHSA-N (2s,3r,4s,5s,6r)-2-[(2r,4r,5r,6s)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2r,4r,5r,6s)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1[C@@H](CO)O[C@@H](OC2[C@H](O[C@H](O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-URKRLVJHSA-N 0.000 description 2
- 229920002498 Beta-glucan Polymers 0.000 description 2
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical group [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 239000004141 Sodium laurylsulphate Substances 0.000 description 2
- 241001136494 Talaromyces funiculosus Species 0.000 description 2
- 239000013543 active substance Substances 0.000 description 2
- 229920002678 cellulose Polymers 0.000 description 2
- 239000001913 cellulose Substances 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 2
- 229920001221 xylan Polymers 0.000 description 2
- 150000004823 xylans Chemical class 0.000 description 2
- 101710130006 Beta-glucanase Proteins 0.000 description 1
- 229920000018 Callose Polymers 0.000 description 1
- 108010059892 Cellulase Proteins 0.000 description 1
- 101000925662 Enterobacteria phage PRD1 Endolysin Proteins 0.000 description 1
- 241000499912 Trichoderma reesei Species 0.000 description 1
- 241000209140 Triticum Species 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 235000004240 Triticum spelta Nutrition 0.000 description 1
- 229920002000 Xyloglucan Polymers 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 229940106157 cellulase Drugs 0.000 description 1
- 230000008602 contraction Effects 0.000 description 1
- 235000019621 digestibility Nutrition 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- KUIXZSYWBHSYCN-UHFFFAOYSA-L remazol brilliant blue r Chemical compound [Na+].[Na+].C1=C(S([O-])(=O)=O)C(N)=C2C(=O)C3=CC=CC=C3C(=O)C2=C1NC1=CC=CC(S(=O)(=O)CCOS([O-])(=O)=O)=C1 KUIXZSYWBHSYCN-UHFFFAOYSA-L 0.000 description 1
- GHMLBKRAJCXXBS-UHFFFAOYSA-N resorcinol Chemical compound OC1=CC=CC(O)=C1 GHMLBKRAJCXXBS-UHFFFAOYSA-N 0.000 description 1
- 238000005507 spraying Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 229920002994 synthetic fiber Polymers 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
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- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Analytical Chemistry (AREA)
- Biotechnology (AREA)
- Physics & Mathematics (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Investigating Or Analysing Materials By The Use Of Chemical Reactions (AREA)
- Apparatus Associated With Microorganisms And Enzymes (AREA)
- Investigating Or Analyzing Non-Biological Materials By The Use Of Chemical Means (AREA)
Abstract
The invention concerns a device for the fast measurement of enzymatic activity in a solid food comprising(i)a container for receiving the sample to be tested;(ii)a reagent particular to the enzyme whereof the activity is to be measured; and(iii)a buffer for placing the enzyme in solution.
Description
The present invention relates to measure fast the device of enzymic activity in the solid feed, comprise that (ⅰ) is used to hold the container of test sample, (ⅱ) enzyme that needs are measured has the specific reagent and (ⅲ) damping fluid of lytic enzyme.
The solid feed that feed does not deal with before preferably measuring.
The feed that is used for livestock industry is supplemented with various enzymes usually, and its effect mainly is a digestibility of improving the feed that gives.These enzymes are sprayed on the feed with liquid form usually, and EP 0,789, and 291 have done special introduction.Enzyme also can add feed by powder type.
Caused two problems like this, first is the homogeneity that inspection adds the enzyme distribution of feed, and second problem is also to assess the activity of the enzyme that adds feed fast easily.Feed producer and wish to check that the raiser that they give the quality of the fodder of animal has proposed these problems especially.Up to now, can under lab measure enzymic activity, cause the nervous and delay of logistics like this, these restrictions are real obstructions when needing as a result at once.
The device of the enzymic activity of any rich enzyme feed of the present invention by being provided for measuring nutrition purposes, especially for feeding animals solves this problem.The measurement of this device is based on colorimetric reaction, can qualitative test and the enzymic activity of sxemiquantitative experiment with measuring sample.
On behalf of the present invention, Fig. 1 be used to measure the embodiment of enzymic activity device, and it is the form of post.
Be described below in conjunction with above-mentioned accompanying drawing.
Enforcement the inventive system comprises the container that is used to hold test sample, needs is measured the damping fluid that its active enzyme has specific reagent and is used to dissolve described enzyme.
The container of this device can be, but is not limited to, by indicating graduated narrow bottom (11) and being used for the post (Fig. 1) that Xiang Zhuli introduces all ingredients and the funnel-shaped top (12) wide to its blended constitutes when stirring.Post also can be equipped with the opening and the closure systems (13) of leakproof, and as stopper, it is connected on the cylinder by tab (tab) (131).
Container also can be made of (Fig. 2) the test tube of single-use.
Container can be made of the synthetic materials such as the single-use plastics.
Container preferably comprises separable projection (14) at its base portion, allows the liquid portion of its inclusion flow out.Advantageously have on the projection and keep nuggets contraction flow region (141) in the feed here.
The measurement of enzymic activity is based on the color reaction of Azo method.The color reaction principle of Azo method is based on the enzymic hydrolysis of the feature substrate of the enzyme that is connected with chromophoric group.Reaction has produced soluble oligopolymer, and it makes medium become blue.Optical density in 590 nanometers measuring media.
The reagent that is used for this device is the substrate by the enzymic catalytic reaction that is connected with chromophoric group.Therefore, enzymatic hydrolysis reaction has discharged chromophoric substrate.
This device also comprises being used to dissolve and is sprayed at the enzyme on the feed and makes enzyme remain on the damping fluid of its optimal ph.
Can mention that (only for exemplifying, not limiting) is used to measure the device of xylanase activity.
In order to measure the activity of zytase, used reagent is " Oat spelt Xylan RemazolBrilliant Blue R " or " Xylazyme AX " (Megazyme company sells, and is made of oat that is connected with dyestuff or wheat araboxylan).
Used damping fluid is selected from acetate/sodium acetate; Glycine hydrochloride/glycine; Equisetic acid/sodium hydroxide; Formic acid/sodium formiate damping fluid.
Also can mention the device that is used to measure 1,4 beta-glucanase activity, this measurement also is based on the color reaction of Azo method.
Spendable substrate is by 1,3: 1, and the 4-callose constitutes, and has Remazol Brilliant BlueR and BetaGlucazyme (being sold by Megazyme company), comprises and zaurine (azurine) bonded beta-glucan.
Used damping fluid is selected from acetate/sodium acetate; Glycine hydrochloride/glycine; Equisetic acid/sodium hydroxide; Formic acid/sodium formiate damping fluid.
In order to measure the activity of cellulase, used substrate is Cellazyme ingot (sale of Megazyme company).These ingots are made of the substrate with zaurine dyestuff polymeric Mierocrystalline cellulose and/or Mierocrystalline cellulose and xyloglucan.
In embodiment preferred of the present invention, reagent is solid form.
Advantageously, for the ease of the enzyme dissolving, can in the substrate that contains chromophoric group reagent, add tensio-active agent.This tensio-active agent is selected from Sodium Lauryl Sulphate BP/USP and sodium lauryl sulphate especially.
The preferable embodiment according to the present invention, measure by following four steps:
-1 milliliter of sample that needs to measure its enzymic activity of introducing in container (1) ,-for solid sample, solid should be filled into 10 milliliters of scale mark places of container;
The reagent of-introducing solid bead form;
Damping fluid to the 20 milliliter scale mark place that-introducing is specific;
-close post with stopper after, with the violent jolting of post for several times.
Can randomly add (by centrifugal or filtration) and separate the additional step of liquid phase and solid phase, with the recovery liquid phase, and by the spectrophotometer measurement colour intensity or simply by relatively measuring colour intensity with colour code (colour scale).
React after 4-8 hour and blue proof to occur and have organized enzyme to exist, colour intensity is directly proportional with the activity of enzyme in being present in sample.
Additional benefit of the present invention is can carry out sxemiquantitative to enzymic activity to measure.Colored liquid phase can reclaim from post by turning off separable projection in the post.Its colour intensity can compare with optical density(OD) (O.D.) working curve.
Except fast, measuring method is also very simple, and device needing Anywhere and not can be used for special equipment.For example, in case made feed, producer or raiser can carry out control survey.
The present invention will do more detailed the elaboration by means of the following example, and these embodiment are used to limit the present invention.
Embodiment
To Rovabio xylan LC (zytase and beta-glucan enzyme mixture, from penicillium funiculosum (Penicillium funiculosum)) and Rovabio zytase TRLC (from the zytase of the mould Trichoderma reesei of wood) carried out the test of two series, their xylanase activity is the 350-550uAXC/ milliliter.The estimation level that the spraying liquid compositions-treated draws on feed is the 70-110uAXC/ kilogram of feed.
Used damping fluid is an acetate buffer, so that pH is remained on 4.7.Sprinkling can be carried out on powdery or granular feed.
| Sample | (before adjusting) activity | Observe after 3 hours | Timesharing in 4 hours 30, the O.D. under the 590nm | In the time of 8 hours, the O.D. under the 590nm | Observe in the time of 8 hours |
| Zytase TRLC on particle | ?1336 | Blue: +++ | ????＞3.0 | ?＞3.0 | Blue: +++ |
| Zytase TRLC on particle | ?886.7 | Blue :+ | ????1.567 | ?2.685 | Blue: ++ |
| Zytase TRLC on particle | ?1469.25 | Blue :+ | ????1.429 | ?2.652 | Blue: ++ |
| Zytase powder before granulating | ?631.4 | No color | ????0.201 | ?0.666 | Blue :+ |
| Zytase LC on particle | ?1144 | Blue: +++ | ????2.309 | ?2.376 | Blue: +++ |
| Zytase LC on particle | ?1386.7 | Blue :+ | ????1.382 | ?2.484 | Blue: +++ |
| Zytase LC on particle | ?1450.5 | Blue: +++ | ????2.872 | ?2.85 | Blue: +++ |
| Zytase LC on particle | ?1330.5 | Blue: ++ | ????1.233 | ?2.096 | Blue: +++ |
Claims (9)
1. a device that is used to measure solid feed sample enzymic activity is characterized in that, it comprises the container that is used to hold test sample, and needs are measured the damping fluid that active enzyme has specific reagent and is used to dissolve described enzyme.
2. device according to claim 1 is characterized in that test sample is a solid feed, does not preferably deal with.
3. device according to claim 1 and 2 is characterized in that, described container is the scale post or the pipe of special purpose, has leakproof opening and closed system.
4. device according to claim 3 is characterized in that, described container is included in the separable projection of its base portion, allows the liquid portion of its content flow out.
5. according to each described device of claim 1-4, it is characterized in that reagent is the substrate of the enzyme that is connected with chromophoric group.
6. according to each described device of claim 1-5, it is characterized in that reagent is solid form or liquid form.
7. device according to claim 1 is characterized in that, the buffer reagent that is used to measure enzymic activity is selected from acetate/sodium acetate; Glycine hydrochloride/glycine; Equisetic acid/sodium hydroxide; Formic acid/sodium formiate damping fluid.
8. the application of device according to claim 1 in the quantitative measurment enzymic activity is characterized in that, the color of gained and typical curve are relatively.
9. a method of measuring enzymic activity in the feed is characterized in that, needs is measured the sample of enzymic activity and is introduced the arbitrary described device of claim 1-5 for 10 milliliters, introduces the reagent of solid bead form; Introduce specific damping fluid and arrive 20 milliliters of scale mark places; Close pillar with stopper, violent jolting for several times; Liquid phase is separated from solid phase, reclaims liquid phase, by relatively measuring colour intensity with colour code.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FR98/10533 | 1998-08-19 | ||
| FR9810533A FR2782523B1 (en) | 1998-08-19 | 1998-08-19 | DEVICE FOR QUICK MEASUREMENT OF ENZYMATIC ACTIVITY |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN1312854A true CN1312854A (en) | 2001-09-12 |
| CN1181182C CN1181182C (en) | 2004-12-22 |
Family
ID=9529765
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CNB998097853A Expired - Lifetime CN1181182C (en) | 1998-08-19 | 1999-08-16 | Fast measuring device of enzymatic activity |
Country Status (19)
| Country | Link |
|---|---|
| US (1) | US6821722B1 (en) |
| EP (1) | EP1105456B1 (en) |
| JP (1) | JP4531258B2 (en) |
| KR (1) | KR20010072751A (en) |
| CN (1) | CN1181182C (en) |
| AT (1) | ATE254169T1 (en) |
| AU (1) | AU752174B2 (en) |
| BR (1) | BR9914294B1 (en) |
| CA (1) | CA2341581C (en) |
| DE (1) | DE69912806T2 (en) |
| DK (1) | DK1105456T3 (en) |
| EA (1) | EA002734B1 (en) |
| ES (1) | ES2209474T3 (en) |
| FR (1) | FR2782523B1 (en) |
| ID (1) | ID28921A (en) |
| MX (1) | MXPA01001628A (en) |
| PT (1) | PT1105456E (en) |
| SA (1) | SA00200919B1 (en) |
| WO (1) | WO2000011136A1 (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20050009116A1 (en) * | 2003-07-07 | 2005-01-13 | Syngenta Participation Ag | Reagents, methods and kit for detecting feed enzymes |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2341865A1 (en) * | 1976-02-19 | 1977-09-16 | Api Labor | SUPPORT FOR THE ASSESSMENT OF ENZYMATIC ACTIVITIES AND METHOD OF ASSESSMENT USING THIS SUPPORT |
| IT8505253A0 (en) * | 1985-11-15 | 1985-11-15 | Copan Srl | SWAB WITH TANK OF TRANSPORT MEDIA FOR COLLECTING AND TRANSFERRING SAMPLES OF SUBSTANCES TO BE ANALYZED INTO TEST. |
| DE69004587T2 (en) * | 1989-02-02 | 1994-05-11 | Abbott Lab | Method and device for quantitative chromatography. |
| JPH04229168A (en) * | 1990-12-26 | 1992-08-18 | Hoechst Japan Ltd | Tool and method for measuring activity of both enzyme and enzymic reaction inhibitor |
| GB2301103B (en) * | 1995-05-23 | 1999-12-22 | Danisco | An enzyme system comprising ferulic acid esterase |
| US6001587A (en) * | 1997-04-08 | 1999-12-14 | The United States Of America As Represented By The Secretary Of The Navy | Chemically specific patterning on solid surfaces using surface immobilized enzymes |
-
1998
- 1998-08-19 FR FR9810533A patent/FR2782523B1/en not_active Expired - Fee Related
-
1999
- 1999-08-16 DE DE69912806T patent/DE69912806T2/en not_active Expired - Lifetime
- 1999-08-16 JP JP2000566393A patent/JP4531258B2/en not_active Expired - Fee Related
- 1999-08-16 AU AU51727/99A patent/AU752174B2/en not_active Expired
- 1999-08-16 PT PT99936736T patent/PT1105456E/en unknown
- 1999-08-16 DK DK99936736T patent/DK1105456T3/en active
- 1999-08-16 BR BRPI9914294-5A patent/BR9914294B1/en not_active IP Right Cessation
- 1999-08-16 KR KR1020017002077A patent/KR20010072751A/en not_active Application Discontinuation
- 1999-08-16 US US09/763,018 patent/US6821722B1/en not_active Expired - Lifetime
- 1999-08-16 MX MXPA01001628A patent/MXPA01001628A/en active IP Right Grant
- 1999-08-16 ES ES99936736T patent/ES2209474T3/en not_active Expired - Lifetime
- 1999-08-16 WO PCT/FR1999/001990 patent/WO2000011136A1/en not_active Application Discontinuation
- 1999-08-16 CN CNB998097853A patent/CN1181182C/en not_active Expired - Lifetime
- 1999-08-16 EP EP99936736A patent/EP1105456B1/en not_active Expired - Lifetime
- 1999-08-16 AT AT99936736T patent/ATE254169T1/en active
- 1999-08-16 EA EA200100247A patent/EA002734B1/en not_active IP Right Cessation
- 1999-08-16 CA CA2341581A patent/CA2341581C/en not_active Expired - Lifetime
- 1999-10-16 ID IDW20010613A patent/ID28921A/en unknown
-
2000
- 2000-02-01 SA SA00200919A patent/SA00200919B1/en unknown
Also Published As
| Publication number | Publication date |
|---|---|
| SA00200919B1 (en) | 2006-06-10 |
| AU5172799A (en) | 2000-03-14 |
| FR2782523A1 (en) | 2000-02-25 |
| US6821722B1 (en) | 2004-11-23 |
| EP1105456B1 (en) | 2003-11-12 |
| ATE254169T1 (en) | 2003-11-15 |
| PT1105456E (en) | 2004-04-30 |
| BR9914294A (en) | 2001-11-06 |
| MXPA01001628A (en) | 2002-04-08 |
| CN1181182C (en) | 2004-12-22 |
| WO2000011136A1 (en) | 2000-03-02 |
| BR9914294B1 (en) | 2011-01-25 |
| DE69912806D1 (en) | 2003-12-18 |
| JP4531258B2 (en) | 2010-08-25 |
| ID28921A (en) | 2001-07-12 |
| FR2782523B1 (en) | 2000-10-06 |
| AU752174B2 (en) | 2002-09-05 |
| CA2341581A1 (en) | 2000-03-02 |
| JP2002523038A (en) | 2002-07-30 |
| EA002734B1 (en) | 2002-08-29 |
| KR20010072751A (en) | 2001-07-31 |
| EP1105456A1 (en) | 2001-06-13 |
| CA2341581C (en) | 2010-10-12 |
| EA200100247A1 (en) | 2001-08-27 |
| ES2209474T3 (en) | 2004-06-16 |
| DE69912806T2 (en) | 2004-09-23 |
| DK1105456T3 (en) | 2004-02-23 |
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